Herpesvirus helicase-primase complex (None established)

The herpesvirus helicase-primase complex is a critical multi-enzyme assembly composed of three subunits: a helicase (e.g., UL5 in HSV-1, pUL105 in HCMV), a primase (e.g., UL52 in HSV-1, pUL70 in HCMV), and a noncatalytic accessory protein (UL8 in HSV-1, pUL102 in HCMV)[1][2][4][5]. The complex unwinds the viral double-stranded DNA and synthesizes short RNA primers required for DNA polymerase-mediated genome replication[1][2][3][5]. Both subunits are essential for viral genome propagation, and inhibitors targeting the helicase-primase are under clinical development for treatment of drug-resistant or recurrent herpesvirus infections[3][6][7]. This complex is highly conserved across the Herpesviridae family, although structural and sequence differences underlie drug sensitivity variation among viral species[4].

Other names

HSV-1 helicase-primase complexHerpes simplex virus helicase-primaseHerpesvirus DNA helicase/primase complexHelicase-primase (UL5/UL52/UL8 for HSV-1, pUL105/pUL70/pUL102 for HCMV)

Inhibition of helicase activity (blocks DNA strand unwinding); Inhibition of primase activity (prevents RNA primer synthesis for replication); Prevents viral DNA replication and proliferation